node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
MCRY_10005 | MCRY_22055 | MCRY_10005 | MCRY_22055 | Molecular chaperone DnaJ; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat shock protein Hsp70; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.996 |
MCRY_10005 | dnaK | MCRY_10005 | MCRY_01895 | Molecular chaperone DnaJ; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.996 |
MCRY_10005 | groEL | MCRY_10005 | MCRY_02835 | Molecular chaperone DnaJ; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.901 |
MCRY_10005 | groS | MCRY_10005 | MCRY_02830 | Molecular chaperone DnaJ; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.689 |
MCRY_10005 | grpE | MCRY_10005 | MCRY_00500 | Molecular chaperone DnaJ; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP [...] | 0.931 |
MCRY_10005 | hslU | MCRY_10005 | MCRY_00690 | Molecular chaperone DnaJ; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.747 |
MCRY_10005 | hslV | MCRY_10005 | MCRY_00695 | Molecular chaperone DnaJ; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.581 |
MCRY_10005 | lon | MCRY_10005 | MCRY_10210 | Molecular chaperone DnaJ; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | DNA-binding protein; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.672 |
MCRY_22055 | MCRY_10005 | MCRY_22055 | MCRY_10005 | Heat shock protein Hsp70; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaJ; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.996 |
MCRY_22055 | dnaJ | MCRY_22055 | MCRY_01900 | Heat shock protein Hsp70; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] | 0.999 |
MCRY_22055 | groEL | MCRY_22055 | MCRY_02835 | Heat shock protein Hsp70; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.978 |
MCRY_22055 | groS | MCRY_22055 | MCRY_02830 | Heat shock protein Hsp70; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.931 |
MCRY_22055 | grpE | MCRY_22055 | MCRY_00500 | Heat shock protein Hsp70; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP [...] | 0.997 |
MCRY_22055 | hslU | MCRY_22055 | MCRY_00690 | Heat shock protein Hsp70; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.724 |
MCRY_22055 | hslV | MCRY_22055 | MCRY_00695 | Heat shock protein Hsp70; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.673 |
MCRY_22055 | lon | MCRY_22055 | MCRY_10210 | Heat shock protein Hsp70; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | DNA-binding protein; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.729 |
dnaJ | MCRY_22055 | MCRY_01900 | MCRY_22055 | Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] | Heat shock protein Hsp70; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
dnaJ | dnaK | MCRY_01900 | MCRY_01895 | Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
dnaJ | groEL | MCRY_01900 | MCRY_02835 | Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.945 |
dnaJ | groS | MCRY_01900 | MCRY_02830 | Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.907 |